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Critical role of HLA-DR?* binding peptides' peripheral flanking residues in fully-protective malaria vaccine development

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dc.creatorReyes C.spa
dc.creatorRojas-Luna R.spa
dc.creatorAza-Conde J.spa
dc.creatorTabares L.spa
dc.creatorPatarroyo M.A.spa
dc.creatorPatarroyo M.E.spa
dc.date.accessioned2020-05-26T00:02:43Z
dc.date.available2020-05-26T00:02:43Z
dc.date.created2017spa
dc.description.abstractA vaccine candidate component must fit perfectly into the antigen presenting HLA-DR?* molecule's groove (or canonical nonapeptide) peptide binding region (PBR) during antigen presentation to the T-cell receptor (TCR), conforming a specific and stable macromolecular complex and induce an appropriate immune response. Antigen's peripheral flanking residues (PFR, positions (p) -p2 and p10) must thus establish strong interactions with the HLA-DR?* - TCR complex. These amino acids (aa) have specific physico-chemical characteristics enabling differentiation between non-protective but antibody-inducer (NPAI), short-lived protection inducer (SLPI) and long-lasting protection inducer (LLPI) peptides when used as an antimalarial vaccine component. Their identification (through 1H-NMR and Aotus monkey immunization) and proper modification contributes to a logical and rational methodology for long-lasting and protective immunological memory. © 2017 Elsevier Inc.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.bbrc.2017.05.123
dc.identifier.issn0006291X
dc.identifier.issn10902104
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23517
dc.language.isoengspa
dc.publisherElsevier B.V.spa
dc.relation.citationEndPage345
dc.relation.citationIssueNo. 3
dc.relation.citationStartPage339
dc.relation.citationTitleBiochemical and Biophysical Research Communications
dc.relation.citationVolumeVol. 489
dc.relation.ispartofBiochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.489, No.3 (2017); pp. 339-345spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85020088359&doi=10.1016%2fj.bbrc.2017.05.123&partnerID=40&md5=5294a25e289db14945da2ebab4f4e0f0spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosariospa
dc.source.reponamereponame:Repositorio Institucional EdocURspa
dc.subject.keywordHLA DR antigenspa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordHLA DRB1 antigenspa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordPeptidespa
dc.subject.keywordAnimal experimentspa
dc.subject.keywordAotusspa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordHydrogen bondspa
dc.subject.keywordImmunogenicityspa
dc.subject.keywordImmunological memoryspa
dc.subject.keywordNonhumanspa
dc.subject.keywordPhysical chemistryspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein structurespa
dc.subject.keywordSequence analysisspa
dc.subject.keywordStructure analysisspa
dc.subject.keywordAnimalspa
dc.subject.keywordAotidaespa
dc.subject.keywordBinding sitespa
dc.subject.keywordChemistryspa
dc.subject.keywordImmunologyspa
dc.subject.keywordSynthesisspa
dc.subject.keywordAnimalsspa
dc.subject.keywordAotidaespa
dc.subject.keywordBinding Sitesspa
dc.subject.keywordHLA-DRB1 Chainsspa
dc.subject.keywordMalaria Vaccinesspa
dc.subject.keywordPeptidesspa
dc.subject.keywordAmino acid side-chain polarityspa
dc.subject.keywordImmune protection-inducing peptide structure (IMPIPS)spa
dc.subject.keywordMHCII-peptide-TCR complexspa
dc.subject.keywordPeripheral flanking residuesspa
dc.titleCritical role of HLA-DR?* binding peptides' peripheral flanking residues in fully-protective malaria vaccine developmentspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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